A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
J. Clin. Invest. Isla Ogilvie, et al. 115:2784 doi:10.1172/JCI26020 [Go to this article.]

Figure 4
Rescue of the complex I assembly defect in patient fibroblasts. (A) BN-PAGE analysis of the complex I assembly defect in the patient (lane A) shows a severe reduction in the activity of the enzyme as measured by an in-gel activity assay (upper panel) and the amount of the holoenzyme as measured by immunoblot analysis of the BN gel using an anti-ND1 antibody (middle panel) compared with control (lane C). Transduction of the patient cells with a retroviral vector expressing the wild-type B17.2L cDNA (lanes A+ B17.2L) completely rescued the biochemical defect. The supercomplex (complex I and III) is labeled α. The lower panel shows an immunoblot of the loading control (70-kDa subunit of complex II). (B) Immunoblot analysis of fibroblasts with an anti-B17.2L antibody showing the complete absence of full-length B17.2L in patient fibroblasts (lane A) compared with control (lane C) and the accumulation of near control levels of the protein after transduction with a retroviral vector expressing the wild-type B17.2L cDNA (lane A+ B17.2L).